Studies on Mono- and Diiodohistidine. I. THE IDENTIFICATION OF IODOHISTIDINES FROM THYROIDAL IODOPROTEINS AND THEIR PERIPHERAL METABOLISM IN THE NORMAL MAN AND RAT

Savoie, J C; Thomopoulos, P; Savoie, F.

doi:10.1172/jci107153

Cited by 30 publications

(20 citation statements)

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“…The general methods applied to the isolation, the separation and the identification of the iodohistidines from the Pronase hydrolysates of the iodoproteins have been described in the preceding paper (12). Briefly, the isolation was made by Dowex 1 chromatography; a partial purification was obtained by butanol partition; the separation of MIH and DIH from each other was obtained by Sephadex G-10 chromatography, and the identification relied upon crystallizations to a constant specific activity.…”

Section: Methodsmentioning

confidence: 99%

“…Urines were analyzed for their iodohistidine content after a 4 N HCl acid hydrolysis at 60°C, for I h (12).…”

Section: Methodsmentioning

confidence: 99%

“…The enzyme was further characterized by determining from goiter homogenates the Km for MIT as previously described (12). The iodotyrosine deiodinase peripheral activity was determined in vivo from labeled MIT or DIT in the conditions described (12).…”

Section: Methodsmentioning

confidence: 99%

“…The iodotyrosine deiodinase peripheral activity was determined in vivo from labeled MIT or DIT in the conditions described (12). The (15); BII from plasma by a modification of a described method (9).…”

Section: Methodsmentioning

confidence: 99%

“…Moreover they were not unique to this variety of congenital goiter since they were detected in the urine of hyperthyroid and thyroid cancer patients treated by 'I. Free monoiodohistidine (MIH) and diiodohistidine (DIH) were identified in the BII moiety of the urine by the methods presented in the preceding paper (12). Therefore the aims of the present study have been: (a) to identify and quantify the iodohistidines excreted in the urine of four patients suffering from this variety of congenital goitrous hypothyroidism; (b) to isolate and identify the iodoproteins from these goiters, with particular consideration given to the thyroglobulin (Tg) content; (c) to determine the iodohistidine and the thyroxine content of these iodoproteins; (d) to detect the presence or absence of an iodotyrosine deiodinase activity.…”

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confidence: 97%

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Studies on Mono- and Diiodohistidine. II. CONGENITAL GOITROUS HYPOTHYROIDISM WITH THYROGLOBULIN DEFECT AND IODOHISTIDINE-RICH IODOALBUMIN PRODUCTION

Savoie¹,

Massin²,

Savoie³

1973

J. Clin. Invest.

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A B S T R A C T Butanol-insoluble iodinated compounds in the urine of patients with congenital goiters have been generally regarded as iodopeptides. Monoiodohistidine (MIH) and diiodohistidine (DIH) were identified from the urine of four patients with congenital goitrous hypothyroidism. From radioiodine studies, 40-70% of the urinary radioactivity was in the iodide-free fraction from which about 40% was identified as MIH and DIH by crystallizations to a constant specific activity.Iodotyrosines were simultaneously identified in the urine. However the presence of an iodotyrosine-deiodinase activity was demonstrated in the two removed goiters with a normal Km for MIT. In vivo iodotyrosine deiodination was normal for hypothyroid subjects.No thyroglobulin was identified in the thyroids from these patients. The major iodoprotein was iodoalbumin which, after in vivo labeling, contained 84-89% of the total soluble protein radioactivity. The thyroxine content of the goiter iodoalbumins and other iodoproteins was extremely low.Iodohistidines were identified in comparable proportions in the iodoalbumin and in the other iodoproteins isolated from each goiter. The average iodohistidine content of these proteins as crystallizable MIH and DIH was in the individual cases 15 and 4% of the in vivo incorporated radioiodine. DIH was identified in all iodoprotein fractions. The mean DIH/MIH ratios from the individual cases were 1.16 and 0.35. The corresponding DIT/MIT ratios were 3.19 and 1.45, respectively.The major consequence of this thyroglobulin defect is the iodination of inappropriate proteins (mainly albumin) resulting in low yields of thyroxine and high Received for publication 6 March 1972 and in revised form 19 September 1972. yields of iodohistidines. Iodohistidines from the goiter iodoproteins were not deiodinated and, at least for MIH, were quantitatively excreted in the urine of these patients. From the MIH iodoalbumin content and the MIH urinary excretion, goiter iodoalbumin turnover estimates were made and, although elevated, could not maintain a normal thyroxine secretion.The urinary excretion of iodohistidines easily demonstrated by column chromatography is offered as a test for detecting this variety of congenital goiter.

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Section: Methodsmentioning

confidence: 99%

“…Urines were analyzed for their iodohistidine content after a 4 N HCl acid hydrolysis at 60°C, for I h (12).…”

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 97%

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Studies on Mono- and Diiodohistidine. II. CONGENITAL GOITROUS HYPOTHYROIDISM WITH THYROGLOBULIN DEFECT AND IODOHISTIDINE-RICH IODOALBUMIN PRODUCTION

Savoie¹,

Massin²,

Savoie³

1973

J. Clin. Invest.

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Halogenated Veneers: Protein Cross‐Linking and Halogenation in the Jaws ofNereis, a Marine Polychaete Worm

et al. 2006

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Mineralized tissues are produced by most living organisms for load and impact functions. In contrast, the jaws of the clam worm, Nereis, are hard without mineralization. However, they are peculiarly rich in halogens, which are associated with a variety of post-translationally modified amino acids, many of which are multiply halogenated by chlorine, bromine, and/or iodine. Several of these modified amino acids, namely dibromohistidine, bromoiodohistidine, chloroiodotyrosine, bromoiodotyrosine, chlorodityrosine, chlorotrityrosine, chlorobromotrityrosine, and bromoiodotrityrosine, have not been previously reported. We have found that the distributions of Cl, Br, and I differ: Cl is widespread whereas Br and I, although not colocalized, are concentrated in proximity to the external jaw surfaces. By using nanoindentation, we show that Br and I are unlikely to play a purely mechanical role, but that the local Zn and Cl concentrations and jaw microstructure are the prime determinants of local jaw hardness. Several of the post-translationally modified amino acids are akin to those found in various sclerotized structures of invertebrates, and we propose that they are part of a cross-linked protein casing.

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Chemical changes accompanying maturation of the connective tissue skeletons of gorgonian and antipatharian corals

Goldberg

1978

Marine Biology

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Studies on Mono- and Diiodohistidine. I. THE IDENTIFICATION OF IODOHISTIDINES FROM THYROIDAL IODOPROTEINS AND THEIR PERIPHERAL METABOLISM IN THE NORMAL MAN AND RAT

Cited by 30 publications

References 33 publications

Studies on Mono- and Diiodohistidine. II. CONGENITAL GOITROUS HYPOTHYROIDISM WITH THYROGLOBULIN DEFECT AND IODOHISTIDINE-RICH IODOALBUMIN PRODUCTION

Studies on Mono- and Diiodohistidine. II. CONGENITAL GOITROUS HYPOTHYROIDISM WITH THYROGLOBULIN DEFECT AND IODOHISTIDINE-RICH IODOALBUMIN PRODUCTION

Halogenated Veneers: Protein Cross‐Linking and Halogenation in the Jaws ofNereis, a Marine Polychaete Worm

Chemical changes accompanying maturation of the connective tissue skeletons of gorgonian and antipatharian corals

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